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Article

Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation.

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis - 1 Sept 1998

Schormann N, Murrell J R, Benson M D

Abstract excerpt

The most common form of hereditary systemic amyloidosis is familial amyloidotic polyneuropathy associated with single amino acid changes in the plasma protein transthyretin. So far, high resolution structures of only three amyloidogenic variants (Met30, Ser84, Ile122) and one non-amyloidogenic variant (Thr109) have been reported complemented by X-ray fiber diffraction studies and image reconstruction from...

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Identifiers

PMID: 9818054
DOI: 10.3109/13506129809003843

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation.PMID 9818054Read ↗

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